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Recombinant Human Bone Morphogenetic Protein-4 produced in E. coli is a a monomeric, non-glycosylated polypeptide chain containing 116 amino acids and having a molecular mass of 13.0 kDa.
Less than 1EU/μg of rHuBMP-4 as determined by LAL method.
>95% by SDS-PAGE and HPLC analyses.
This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
PDB rendering based on 1reu
Human BMP-4 is one of at least 15 structurally and functionally related BMPs, which are members of the transforming growth factor β (TGF-β) superfamily. BMPs were originally identified as protein regulators of cartilage and bone formation. However, they havesince been shown to be involved in embryogenesis and morphogenesis of various tissues and organs. BMPs have also been shown to regulate the growth, differentiation, chemotaxis and apoptosis of various cell types, including mesenchymal cells, epithelial cells, hematopoietic cells and neuronal cells. BMP-4 is synthesized as large precursor molecules which are cleaved by proteolytic enzymes. The active form can consist of a dimer of two identical proteins or a heterodimer of two related bone morphogenetic proteins.
cytokine activity. growth factor activity. heparin binding. protein binding. signal transducer activity.